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Volumn 104, Issue 1, 2012, Pages 65-71

Physiological effect of chitinase purified from Bacillus subtilis against the tobacco cutworm Spodoptera litura Fab

Author keywords

Bacillus; Chitinase; Cutworm; Dietary utilization; Enzyme; Molecular masses; Mortality

Indexed keywords

BACILLUS SUBTILIS; NICOTIANA TABACUM; SPODOPTERA LITURA;

EID: 84865802143     PISSN: 00483575     EISSN: 10959939     Source Type: Journal    
DOI: 10.1016/j.pestbp.2012.07.002     Document Type: Article
Times cited : (74)

References (58)
  • 1
    • 0027331112 scopus 로고
    • Making greater use of introduced microorganisms for biological control of plant pathogens
    • Cook R.J. Making greater use of introduced microorganisms for biological control of plant pathogens. Annu. Rev. Phytopathol. 1993, 3:53-80.
    • (1993) Annu. Rev. Phytopathol. , vol.3 , pp. 53-80
    • Cook, R.J.1
  • 2
    • 0033290707 scopus 로고    scopus 로고
    • Chitinases in biological control
    • Herrera-Estrella A., Chet I. Chitinases in biological control. EXS 1999, 87:171-184.
    • (1999) EXS , vol.87 , pp. 171-184
    • Herrera-Estrella, A.1    Chet, I.2
  • 3
    • 68949189398 scopus 로고    scopus 로고
    • Effects of Jasmonic acid-induced resistance in rice on the plant brownhopper, Nilaparvata lugens Stål (Homoptera: Delphacidae)
    • Senthil-Nathan S., Kalaivani K., Choi M.Y., Paik C.H. Effects of Jasmonic acid-induced resistance in rice on the plant brownhopper, Nilaparvata lugens Stål (Homoptera: Delphacidae). Pest. Biochem. Physiol. 2009, 95:77-84.
    • (2009) Pest. Biochem. Physiol. , vol.95 , pp. 77-84
    • Senthil-Nathan, S.1    Kalaivani, K.2    Choi, M.Y.3    Paik, C.H.4
  • 4
    • 33748333185 scopus 로고    scopus 로고
    • Combined effects of azadirachtin and nucleopolyhedrovirus (SpltNPV) on Spodoptera litura Fabricius (Lepidoptera: Noctuidae) larvae
    • Senthil-Nathan S., Kalaivani K. Combined effects of azadirachtin and nucleopolyhedrovirus (SpltNPV) on Spodoptera litura Fabricius (Lepidoptera: Noctuidae) larvae. Biol. Control 2006, 36:94-104.
    • (2006) Biol. Control , vol.36 , pp. 94-104
    • Senthil-Nathan, S.1    Kalaivani, K.2
  • 5
    • 23844450461 scopus 로고    scopus 로고
    • The effects of Azadirachtin and Nucleopolyhedrovirus (NPV) on midgut enzymatic profile of Spodoptera litura Fab
    • S. Senthil-Nathan, K. Kalaivani, P.G. Chung, The effects of Azadirachtin and Nucleopolyhedrovirus (NPV) on midgut enzymatic profile of Spodoptera litura Fab. (Lepidoptera: Noctuidae), Pest. Biochem. Physiol. 83 (2005) 46-57.
    • (2005) (Lepidoptera: Noctuidae), Pest. Biochem. Physiol. , vol.83 , pp. 46-57
    • Senthil-Nathan, S.1    Kalaivani, K.2    Chung, P.G.3
  • 7
    • 33745039979 scopus 로고    scopus 로고
    • Review of fungal chitinases
    • Chuan D.L. Review of fungal chitinases. Mycopathologia 2006, 161:345-360.
    • (2006) Mycopathologia , vol.161 , pp. 345-360
    • Chuan, D.L.1
  • 8
    • 73849110534 scopus 로고    scopus 로고
    • Insect chitinase and chitinase-like proteins
    • Arakane Y., Muthukrishnan S. Insect chitinase and chitinase-like proteins. Cell Mol. Life Sci. 2009, 67:201-216.
    • (2009) Cell Mol. Life Sci. , vol.67 , pp. 201-216
    • Arakane, Y.1    Muthukrishnan, S.2
  • 9
    • 0344110241 scopus 로고    scopus 로고
    • Insect Chitinases: molecular biology and potential use as Biopesticides
    • Kramer K.J., Muthukrishnan S. Insect Chitinases: molecular biology and potential use as Biopesticides. Insect Biochem. Mol. Biol. 1997, 27:887-900.
    • (1997) Insect Biochem. Mol. Biol. , vol.27 , pp. 887-900
    • Kramer, K.J.1    Muthukrishnan, S.2
  • 10
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B., Bairoch A. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 1993, 293:781-788.
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 11
    • 37149036918 scopus 로고    scopus 로고
    • Fungal chitinases
    • (Ed.), Biotechnology Department, Lab. Biopolymers. Av. San Rafael Atlixco No. 186. Col. Vicentina, Mexico.
    • K.S. Matsumoto (Ed.), Fungal chitinases. Biotechnology Department, Lab. Biopolymers. Av. San Rafael Atlixco No. 186. (2006), Col. Vicentina, Mexico.
    • (2006)
    • Matsumoto, K.S.1
  • 12
    • 0346399742 scopus 로고    scopus 로고
    • Chitin metabolism in insects: structure, function and regulation of chitin synthases and chitinases
    • Merzendorfer H., Zimoch L. Chitin metabolism in insects: structure, function and regulation of chitin synthases and chitinases. J. Exp. Biol. 2003, 206:4393-4412.
    • (2003) J. Exp. Biol. , vol.206 , pp. 4393-4412
    • Merzendorfer, H.1    Zimoch, L.2
  • 14
    • 10744227010 scopus 로고    scopus 로고
    • Suppression of leaf feeding and oviposition of phytophagous ladybird beetles by chitinase gene-transformed phylloplane bacteria and their specific bacteriophages entrapped in alginate gel beads
    • Otsu Y., Mori H., Komuta K., Shimizu H., Nogawa S., Matsuda Y., Nonomura T., Sakurarani Y., Tosa S., Mayama S., Toyoda H. Suppression of leaf feeding and oviposition of phytophagous ladybird beetles by chitinase gene-transformed phylloplane bacteria and their specific bacteriophages entrapped in alginate gel beads. J. Econ. Entomol. 2003, 96:555-563.
    • (2003) J. Econ. Entomol. , vol.96 , pp. 555-563
    • Otsu, Y.1    Mori, H.2    Komuta, K.3    Shimizu, H.4    Nogawa, S.5    Matsuda, Y.6    Nonomura, T.7    Sakurarani, Y.8    Tosa, S.9    Mayama, S.10    Toyoda, H.11
  • 15
    • 4744343733 scopus 로고    scopus 로고
    • Cloning, expression and functional characterization of chitinase from larvae of tomato moth (Lacanobia oleracea): a demonstration of the insecticidal activity of insect chitinase
    • Fitches E., Wilkerson H., Bell H., Bown D.P., Gatehouse J.A., Edwards J.P. Cloning, expression and functional characterization of chitinase from larvae of tomato moth (Lacanobia oleracea): a demonstration of the insecticidal activity of insect chitinase. Insect Biochem. Mol. Biol. 2004, 34:1037-1050.
    • (2004) Insect Biochem. Mol. Biol. , vol.34 , pp. 1037-1050
    • Fitches, E.1    Wilkerson, H.2    Bell, H.3    Bown, D.P.4    Gatehouse, J.A.5    Edwards, J.P.6
  • 16
    • 33748885083 scopus 로고    scopus 로고
    • Bioconversion of shellfish chitin waste for the production of Bacillus subtilis W-188 chitinase
    • Wang S.L., Lin T.Y., Yen Y.H., Liao H.F., Chen Y.J. Bioconversion of shellfish chitin waste for the production of Bacillus subtilis W-188 chitinase. Carbohydr. Res. 2006, 34:2507-2515.
    • (2006) Carbohydr. Res. , vol.34 , pp. 2507-2515
    • Wang, S.L.1    Lin, T.Y.2    Yen, Y.H.3    Liao, H.F.4    Chen, Y.J.5
  • 18
    • 0024662890 scopus 로고
    • Chitinase and chitobiase production during fermentation of genetically improved Serratia liquefaciens
    • Loshi S., Kozlowski M., Richens S., Comberbach D.M. Chitinase and chitobiase production during fermentation of genetically improved Serratia liquefaciens. Enzyme Microb. Technol. 1989, 11:289-296.
    • (1989) Enzyme Microb. Technol. , vol.11 , pp. 289-296
    • Loshi, S.1    Kozlowski, M.2    Richens, S.3    Comberbach, D.M.4
  • 19
    • 0030759788 scopus 로고    scopus 로고
    • Gram-scale synthesis of recombinant chitooligosaccharides in Escherichia coli
    • Samain E., Drouillard S., Heyraud A., Driguez H., Geremia R.A. Gram-scale synthesis of recombinant chitooligosaccharides in Escherichia coli. Carbohydr. Res. 1997, 302:35-42.
    • (1997) Carbohydr. Res. , vol.302 , pp. 35-42
    • Samain, E.1    Drouillard, S.2    Heyraud, A.3    Driguez, H.4    Geremia, R.A.5
  • 20
    • 1942538348 scopus 로고    scopus 로고
    • Developments in the use of Bacillus species for industrial production
    • Schallmey M., Singh A., Ward O.P. Developments in the use of Bacillus species for industrial production. Can. J. Microbiol. 2004, 50:1-17.
    • (2004) Can. J. Microbiol. , vol.50 , pp. 1-17
    • Schallmey, M.1    Singh, A.2    Ward, O.P.3
  • 21
    • 55549131112 scopus 로고    scopus 로고
    • Cloning and expression of an antifungal chitinase gene of a novel Bacillus subtilis isolate from Taiwan potato field
    • Yang C.Y., Hoa Y.C., Pang J.C., Huang S.S., Tschen J.S.M. Cloning and expression of an antifungal chitinase gene of a novel Bacillus subtilis isolate from Taiwan potato field. Biores. Technol. 2009, 100:1454-1458.
    • (2009) Biores. Technol. , vol.100 , pp. 1454-1458
    • Yang, C.Y.1    Hoa, Y.C.2    Pang, J.C.3    Huang, S.S.4    Tschen, J.S.M.5
  • 22
    • 4143127722 scopus 로고    scopus 로고
    • Purification and characterization of chitosanase from Bacillus spp. strain KCTC 0377BP and its application for the production of chitosan oligosaccharides
    • Y.J. Choi, E.J. Kim, Z. Piao, Y.C. Yun, Y.C. Shin, Purification and characterization of chitosanase from Bacillus spp. strain KCTC 0377BP and its application for the production of chitosan oligosaccharides, Appl. Environ. Microbiol. (2004) 4522-4531.
    • (2004) Appl. Environ. Microbiol. , pp. 4522-4531
    • Choi, Y.J.1    Kim, E.J.2    Piao, Z.3    Yun, Y.C.4    Shin, Y.C.5
  • 23
    • 79951736267 scopus 로고
    • Synthetic pyrethroids and other bait formulation in the control of Spodoptera litura (Fab.) attacking rabi groundnut
    • V.V. Ramana, G.P.V. Reddy, M.M. Krishnamurthy, Synthetic pyrethroids and other bait formulation in the control of Spodoptera litura (Fab.) attacking rabi groundnut, Pesticides 1 (1988) 13-16.
    • (1988) Pesticides , vol.1 , pp. 13-16
    • Ramana, V.V.1    Reddy, G.P.V.2    Krishnamurthy, M.M.3
  • 24
    • 21844520865 scopus 로고
    • Analysis of damage to soyabeans infested by the common cutworm, Spodoptera litura Fabricius (Lepidoptera: Noctuidae). II. Estimation of leaf area damaged by young larvae using spectral reflectivity
    • Higuchi H., Yamamoto H., Suzuki Y. Analysis of damage to soyabeans infested by the common cutworm, Spodoptera litura Fabricius (Lepidoptera: Noctuidae). II. Estimation of leaf area damaged by young larvae using spectral reflectivity. Jpn. J. Appl. Entomol. Zool. 1994, 38:297-300.
    • (1994) Jpn. J. Appl. Entomol. Zool. , vol.38 , pp. 297-300
    • Higuchi, H.1    Yamamoto, H.2    Suzuki, Y.3
  • 25
    • 4644363539 scopus 로고    scopus 로고
    • Protein metabolism in Spodoptera litura (F.) is influenced by the botanical insecticide azadirachtin
    • Z. Huang, P. Shi, J. Dai, J. Du, Protein metabolism in Spodoptera litura (F.) is influenced by the botanical insecticide azadirachtin, Pest. Biochem. Physiol. 80 (2004) 85-93.
    • (2004) Pest. Biochem. Physiol. , vol.80 , pp. 85-93
    • Huang, Z.1    Shi, P.2    Dai, J.3    Du, J.4
  • 27
    • 0014540906 scopus 로고
    • The chitinase of Serratia marcescens
    • Monreal J., Reese E.T. The chitinase of Serratia marcescens. Can. J. Microbiol. 1969, 15:689-696.
    • (1969) Can. J. Microbiol. , vol.15 , pp. 689-696
    • Monreal, J.1    Reese, E.T.2
  • 29
    • 84986946216 scopus 로고
    • Assessment of in vitro screening systems for potential biocontrol agents of Gaeumannomyces graminis
    • Renwick A., Campbell R., Coe S. Assessment of in vitro screening systems for potential biocontrol agents of Gaeumannomyces graminis. Plant Pathol. 1991, 40:524-532.
    • (1991) Plant Pathol. , vol.40 , pp. 524-532
    • Renwick, A.1    Campbell, R.2    Coe, S.3
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of Bacteriophage T4
    • Lemmli U.K. Cleavage of structural proteins during the assembly of the head of Bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Lemmli, U.K.1
  • 31
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller G.L. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 1959, 31:426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 32
    • 74549188461 scopus 로고    scopus 로고
    • Purification and characterization of two extracellular endochitinases from Massilia timonae
    • Adrangi S., Faramarzi M., Shahverdi A.R., Sepehrizadeh Z. Purification and characterization of two extracellular endochitinases from Massilia timonae. Carbohydr. Res. 2010, 345:402-407.
    • (2010) Carbohydr. Res. , vol.345 , pp. 402-407
    • Adrangi, S.1    Faramarzi, M.2    Shahverdi, A.R.3    Sepehrizadeh, Z.4
  • 34
    • 0000722909 scopus 로고
    • A method for computing the effectiveness of an insecticide
    • Abbott W.S. A method for computing the effectiveness of an insecticide. J. Econ. Entomol. 1925, 18:265-267.
    • (1925) J. Econ. Entomol. , vol.18 , pp. 265-267
    • Abbott, W.S.1
  • 36
    • 0000440964 scopus 로고
    • The consumption, digestion and utilization of solanaceous and non-solanaceous plants by larvae of the tobacco hornworm, Protoparce sexta (Johan.) (Lepidoptera: Sphingidae)
    • Waldbauer G.P. The consumption, digestion and utilization of solanaceous and non-solanaceous plants by larvae of the tobacco hornworm, Protoparce sexta (Johan.) (Lepidoptera: Sphingidae). Entomol. Exp. Appl. 1964, 7:253-269.
    • (1964) Entomol. Exp. Appl. , vol.7 , pp. 253-269
    • Waldbauer, G.P.1
  • 37
    • 0001300769 scopus 로고
    • Enhancement of baculovirus activity on gypsy moth (Lepidoptera; Lymantriidae) by chitinase
    • Shapiro M., Preisler H.K., Robertson J.I. Enhancement of baculovirus activity on gypsy moth (Lepidoptera; Lymantriidae) by chitinase. J. Econ. Entomol. 1987, 80:1113-1116.
    • (1987) J. Econ. Entomol. , vol.80 , pp. 1113-1116
    • Shapiro, M.1    Preisler, H.K.2    Robertson, J.I.3
  • 38
    • 0242722986 scopus 로고    scopus 로고
    • Isolation of chitin-utilizing bacterium and production of its extracellular chitinase
    • Woo C.J., Yun U.J., Park H.D. Isolation of chitin-utilizing bacterium and production of its extracellular chitinase. J. Microbiol. Biotech. 1996, 6:439-444.
    • (1996) J. Microbiol. Biotech. , vol.6 , pp. 439-444
    • Woo, C.J.1    Yun, U.J.2    Park, H.D.3
  • 39
    • 0036307394 scopus 로고    scopus 로고
    • Purification, characterization and cloning of a chitinase from Bacillus spp. NCTU2
    • Wen C.M., Tseng C.S., Cheng C.Y., Li Y.K. Purification, characterization and cloning of a chitinase from Bacillus spp. NCTU2. Biotechnol. Appl. Biochem. 2002, 35:213-219.
    • (2002) Biotechnol. Appl. Biochem. , vol.35 , pp. 213-219
    • Wen, C.M.1    Tseng, C.S.2    Cheng, C.Y.3    Li, Y.K.4
  • 42
    • 0033982479 scopus 로고    scopus 로고
    • Purification and characterization of a 49-kDa chitinase from Streptomyces griseus HUT 6037
    • Tanabe T., Kawase T., Watanabe T., Uchida Y., Mitsutomi M. Purification and characterization of a 49-kDa chitinase from Streptomyces griseus HUT 6037. J. Biosci. Bioeng. 2000, 89:27-32.
    • (2000) J. Biosci. Bioeng. , vol.89 , pp. 27-32
    • Tanabe, T.1    Kawase, T.2    Watanabe, T.3    Uchida, Y.4    Mitsutomi, M.5
  • 43
    • 0027297246 scopus 로고
    • Chitinases of fungi and plants: their involvement in morphogenesis and host parasite interaction
    • Sahai A.S., Manocha M.S. Chitinases of fungi and plants: their involvement in morphogenesis and host parasite interaction. FEMS Microbiol. Rev. 1993, 11:317-338.
    • (1993) FEMS Microbiol. Rev. , vol.11 , pp. 317-338
    • Sahai, A.S.1    Manocha, M.S.2
  • 44
    • 0016163163 scopus 로고
    • Three year of aerial field experiments with Bacillus thuringiensis plus chitinase formulation against the spruce bud worm
    • Smirnoff W.A. Three year of aerial field experiments with Bacillus thuringiensis plus chitinase formulation against the spruce bud worm. J. Invert Pathol. 1974, 24:344-348.
    • (1974) J. Invert Pathol. , vol.24 , pp. 344-348
    • Smirnoff, W.A.1
  • 45
    • 0002779515 scopus 로고
    • The peritrophic membrane: ultrastructural analysis and function as a mechanical barrier to microbial infection in Orgyia pseudotsugata
    • Brandt C.R., Adang M.J., Spence K.D. The peritrophic membrane: ultrastructural analysis and function as a mechanical barrier to microbial infection in Orgyia pseudotsugata. J. Invert Pathol. 1978, 32:12-24.
    • (1978) J. Invert Pathol. , vol.32 , pp. 12-24
    • Brandt, C.R.1    Adang, M.J.2    Spence, K.D.3
  • 46
    • 0027668880 scopus 로고
    • Sequence of a cDNA and expression of the gene encoding epidermal and gut chitinases of Manduca sexta
    • Kramer K.J., Corpuz L., Choi H.K., Muthukrishnan S. Sequence of a cDNA and expression of the gene encoding epidermal and gut chitinases of Manduca sexta. Insect Biochem. Mol. Biol. 1993, 23:691-701.
    • (1993) Insect Biochem. Mol. Biol. , vol.23 , pp. 691-701
    • Kramer, K.J.1    Corpuz, L.2    Choi, H.K.3    Muthukrishnan, S.4
  • 47
    • 0036891089 scopus 로고    scopus 로고
    • Presence of chitinase and β-N-acetylglucosaminidase in the Aedes aegypti, a chitinolytic system involving peritrophic matrix formation and degradation
    • Filho B.P., Lemos F.J., Secundino N.F., Pascoa V., Pereira S.T., Pimenta P.F. Presence of chitinase and β-N-acetylglucosaminidase in the Aedes aegypti, a chitinolytic system involving peritrophic matrix formation and degradation. Insect Biochem. Mol. Biol. 2002, 32:1723-1729.
    • (2002) Insect Biochem. Mol. Biol. , vol.32 , pp. 1723-1729
    • Filho, B.P.1    Lemos, F.J.2    Secundino, N.F.3    Pascoa, V.4    Pereira, S.T.5    Pimenta, P.F.6
  • 49
  • 51
    • 84971922503 scopus 로고
    • Characteristic of a highly concentrated Bacillus thuringiensis formulation against spruce budworm, Choristoneura fumiferana (Lepidoptera: Tortricidae)
    • Smirnoff W.A., Valero J.R. Characteristic of a highly concentrated Bacillus thuringiensis formulation against spruce budworm, Choristoneura fumiferana (Lepidoptera: Tortricidae). Can. Entomol. 1983, 115:443-444.
    • (1983) Can. Entomol. , vol.115 , pp. 443-444
    • Smirnoff, W.A.1    Valero, J.R.2
  • 52
    • 74049139078 scopus 로고    scopus 로고
    • Purification and partial characterization of a 36-kDa chitinase from Bacillus thuringiensis subsp. colmeri, and its biocontrol potential
    • D. Liu, J. Cai, C.C. Xie, C. Liu, Y.H. Chen, Purification and partial characterization of a 36-kDa chitinase from Bacillus thuringiensis subsp. colmeri, and its biocontrol potential, Enzyme Microb. Technol. 46 (2010) 252-256.
    • (2010) Enzyme Microb. Technol. , vol.46 , pp. 252-256
    • Liu, D.1    Cai, J.2    Xie, C.C.3    Liu, C.4    Chen, Y.H.5
  • 53
    • 0030574272 scopus 로고    scopus 로고
    • Expression of chitinase-encoding genes from Aeromonas hydrophila and Pseudomonas maltophila in Bacillus thuringiensis subsp. israelensis
    • C. Wiwat, M. Lertcanawanichakul, P. Siwayapram, S. Pantuwatana, A. Bhumiratana, Expression of chitinase-encoding genes from Aeromonas hydrophila and Pseudomonas maltophila in Bacillus thuringiensis subsp. israelensis. Gene 179 (1996) 119-126.
    • (1996) Gene , vol.179 , pp. 119-126
    • Wiwat, C.1    Lertcanawanichakul, M.2    Siwayapram, P.3    Pantuwatana, S.4    Bhumiratana, A.5
  • 54
    • 0002577185 scopus 로고
    • Improvement of the insecticidal activity of Bacillus thuringiensis var. entomocidus on larvae of Spodoptera littoralis (Lepidoptera, Noctuidae) by addition of chitinolytic bacteria, a phagostimulant and a UV-protectant
    • B. Sneh, S. Schuster, S. Gross, Improvement of the insecticidal activity of Bacillus thuringiensis var. entomocidus on larvae of Spodoptera littoralis (Lepidoptera, Noctuidae) by addition of chitinolytic bacteria, a phagostimulant and a UV-protectant. Z. ang, Entomology 96 (1983) 77-83.
    • (1983) Z. ang, Entomology , vol.96 , pp. 77-83
    • Sneh, B.1    Schuster, S.2    Gross, S.3
  • 55
    • 0027208132 scopus 로고
    • Chitinase: a novel target for blocking parasite transmission?
    • Shahabuddin M., Kaslow D.C. Chitinase: a novel target for blocking parasite transmission?. Parasitol. Today 1993, 9:252-255.
    • (1993) Parasitol. Today , vol.9 , pp. 252-255
    • Shahabuddin, M.1    Kaslow, D.C.2
  • 56
    • 34248398420 scopus 로고    scopus 로고
    • Food consumption, utilization and detoxification enzyme activity of the rice leaffolder larvae after treatment with Dysoxylum limonoids
    • Senthil-Nathan S., Choi M.Y., Paik C.H., Seo H.Y. Food consumption, utilization and detoxification enzyme activity of the rice leaffolder larvae after treatment with Dysoxylum limonoids. Pest. Biochem. Physiol. 2007, 88(3):260-267.
    • (2007) Pest. Biochem. Physiol. , vol.88 , Issue.3 , pp. 260-267
    • Senthil-Nathan, S.1    Choi, M.Y.2    Paik, C.H.3    Seo, H.Y.4
  • 57
    • 11844281504 scopus 로고    scopus 로고
    • The toxicity and physiological effect of neem limonoids on Cnaphalocrocis medinalis (Guenée) the rice leaffolder
    • Senthil-Nathan S., Kalaivani K., Murugan K., Chung P.G. The toxicity and physiological effect of neem limonoids on Cnaphalocrocis medinalis (Guenée) the rice leaffolder. Pest. Biochem. Physiol. 2005, 81(2):113-122.
    • (2005) Pest. Biochem. Physiol. , vol.81 , Issue.2 , pp. 113-122
    • Senthil-Nathan, S.1    Kalaivani, K.2    Murugan, K.3    Chung, P.G.4
  • 58
    • 27744560294 scopus 로고    scopus 로고
    • Efficacy of neem limonoids on Cnaphalocrocis medinalis (Guenée) (Lepidoptera: Pyralidae) the rice leaffolder
    • S. Senthil-Nathan, K. Kalaivani, K. Murugan, P.G. Chung, Efficacy of neem limonoids on Cnaphalocrocis medinalis (Guenée) (Lepidoptera: Pyralidae) the rice leaffolder. Crop Prot. 24 (2005) 760-763.
    • (2005) Crop Prot. , vol.24 , pp. 760-763
    • Senthil-Nathan, S.1    Kalaivani, K.2    Murugan, K.3    Chung, P.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.